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HEADER HYDROLASE 03-FEB-11 3QM1
TITLE CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
TITLE 2 LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE, FORM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 22-265;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS JOHNSONII;
SOURCE 3 ORGANISM_TAXID: 33959;
SOURCE 4 GENE: LJ0536;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV-L
KEYWDS ALPHA/BETA HYDROLASE FOLD, CINNAMOYL/FERULOYL ESTERASE,
KEYWDS 2 HYDROXYCINAMMATES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,K.K.LAI,C.VU,X.XU,H.CUI,S.MOLLOY,C.F.GONZALEZ,A.YAKUNIN,
AUTHOR 2 A.SAVCHENKO
REVDAT 1 31-AUG-11 3QM1 0
JRNL AUTH K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,A.MOLLOY,A.SAVCHENKO,
JRNL AUTH 2 A.YAKUNIN,C.F.GONZALEZ
JRNL TITL AN INSERTED α/β SUBDOMAIN SHAPES THE CATALYTIC
JRNL TITL 2 POCKET OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
JRNL REF PLOS ONE 2011
JRNL REFN ESSN 1932-6203
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 22353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 23.0686 - 3.6294 1.00 2836 150 0.1391 0.1664
REMARK 3 2 3.6294 - 2.8825 1.00 2740 145 0.1405 0.1783
REMARK 3 3 2.8825 - 2.5186 0.99 2688 140 0.1529 0.2021
REMARK 3 4 2.5186 - 2.2886 0.98 2666 138 0.1422 0.2115
REMARK 3 5 2.2886 - 2.1247 0.98 2631 141 0.1385 0.1890
REMARK 3 6 2.1247 - 1.9995 0.98 2608 137 0.1392 0.2088
REMARK 3 7 1.9995 - 1.8994 0.95 2560 135 0.1636 0.1941
REMARK 3 8 1.8994 - 1.8168 0.94 2505 133 0.2268 0.2669
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 42.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.40240
REMARK 3 B22 (A**2) : -2.42420
REMARK 3 B33 (A**2) : -0.97820
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.016 2056
REMARK 3 ANGLE : 1.710 2809
REMARK 3 CHIRALITY : 0.116 320
REMARK 3 PLANARITY : 0.010 371
REMARK 3 DIHEDRAL : 13.380 760
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resid -5:179
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4870 11.4229 -7.4499
REMARK 3 T TENSOR
REMARK 3 T11: 0.0828 T22: 0.0923
REMARK 3 T33: 0.1351 T12: 0.0051
REMARK 3 T13: 0.0380 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.4086 L22: 1.7207
REMARK 3 L33: 0.2404 L12: 0.2283
REMARK 3 L13: 0.0093 L23: -0.6127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: 0.0146 S13: 0.0181
REMARK 3 S21: -0.2004 S22: -0.0690 S23: -0.3415
REMARK 3 S31: 0.0450 S32: 0.0197 S33: 0.0879
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resid 180:244
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5993 18.5354 -13.7587
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.1082
REMARK 3 T33: 0.0946 T12: -0.0029
REMARK 3 T13: -0.0131 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 1.8123
REMARK 3 L33: 0.9886 L12: -0.2012
REMARK 3 L13: 0.2229 L23: -0.9612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: 0.0422 S13: 0.0724
REMARK 3 S21: -0.2784 S22: 0.0627 S23: 0.1516
REMARK 3 S31: 0.0905 S32: -0.1782 S33: -0.0837
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 23.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 FOR THE DATA SET : 27.5600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32600
REMARK 200 FOR SHELL : 3.180
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB CODE 3PF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M AMMONIUM
REMARK 280 SULPHATE, 24% PEG3350, 25 MM ETHYL FERULATE, 1/10 V8 PROTEASE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.57100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.57100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.93600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.69800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.93600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.69800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.57100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.93600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.69800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.57100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.93600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.69800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A 302 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 456 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 78 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 9 -129.04 57.58
REMARK 500 ALA A 36 -159.52 -94.44
REMARK 500 ARG A 98 -80.86 -95.79
REMARK 500 ALA A 106 -120.20 63.73
REMARK 500 HIS A 153 73.27 -155.56
REMARK 500 LYS A 161 -125.38 57.20
REMARK 500 ASP A 229 -114.51 53.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 466 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH A 467 DISTANCE = 5.35 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE BOND ANGLE OAL-CAM-OAC, WITH A VALUE OF 116 DEGREES, IS MODELED
REMARK 600 IN UNAMBIGUOUS ELECTRON DENSITY TO CONTAIN PARTIAL CHIRAL CHARACTER
REMARK 600 PERHAPS DUE TO THE FACT THAT THIS LIGAND IS BOUND TO A
REMARK 600 CATALYTICALLY INACTIVE MUTANT, S106A, OF THE LJ0536 ENZYME. BOND IS
REMARK 600 STRAINED FROM IDEAL OF 120 DEGREES AS ENZYME COULD HAVE TRAPPED
REMARK 600 SUBSTRATE IN A PSEUDO-TRANSITION STATE OF THE HYDROLYSIS REACTION,
REMARK 600 PRESUMED TO CONTAIN A TETRAHEDRAL TRANSITION STATE WITH A OAL-CAM-
REMARK 600 OAC BOND ANGLE OF 109 DEGREES
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 282 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 479 O
REMARK 620 2 ASP A 209 O 158.4
REMARK 620 3 TYR A 212 O 94.3 107.1
REMARK 620 4 SER A 215 OG 93.4 83.5 106.6
REMARK 620 5 HOH A 385 O 103.8 77.5 80.5 161.0
REMARK 620 6 HOH A 438 O 71.7 86.9 166.0 74.6 102.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 276 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 63 OD1
REMARK 620 2 LYS A 71 O 116.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 246 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 439 O
REMARK 620 2 HOH A 469 O 101.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 263 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 388 O
REMARK 620 2 HOH A 353 O 119.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 275 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 413 O
REMARK 620 2 HOH A 388 O 91.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 257 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 447 O
REMARK 620 2 GLN A -1 O 110.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 250 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 423 O
REMARK 620 2 HOH A 476 O 136.1
REMARK 620 3 HOH A 407 O 155.1 68.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 255 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 67 O
REMARK 620 2 ASP A 69 OD1 115.6
REMARK 620 3 GLN A 12 OE1 128.5 115.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 267 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 348 O
REMARK 620 2 HOH A 467 O 137.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 253 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 362 O
REMARK 620 2 GLN A 175 O 120.1
REMARK 620 3 HOH A 344 O 120.7 110.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 258 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 157 O
REMARK 620 2 HOH A 441 O 114.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 283 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 422 O
REMARK 620 2 HOH A 411 O 91.2
REMARK 620 3 HOH A 352 O 103.5 115.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 280 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 196 OD2
REMARK 620 2 GLY A 222 O 72.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 271 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 149 O
REMARK 620 2 GLY A 142 O 65.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 285 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 209 OD2
REMARK 620 2 HOH A 426 O 87.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYC A 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 291
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PF8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536
REMARK 900 RELATED ID: 3PF9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT
REMARK 900 RELATED ID: 3PFA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID
REMARK 900 RELATED ID: 3PFB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE
REMARK 900 RELATED ID: 3PFC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 MUTANT IN COMPLEX WITH FERULIC ACID
DBREF 3QM1 A 1 244 UNP D3YEX6 D3YEX6_LACJO 1 244
SEQADV 3QM1 MET A -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 GLY A -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 SER A -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 SER A -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 HIS A -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 SER A -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 SER A -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 GLY A -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 ARG A -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 GLU A -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 ASN A -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 LEU A -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 TYR A -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 PHE A -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 GLN A -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 GLY A 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3QM1 ALA A 106 UNP D3YEX6 SER 106 ENGINEERED MUTATION
SEQRES 1 A 265 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 265 ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR
SEQRES 3 A 265 LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU
SEQRES 4 A 265 GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE
SEQRES 5 A 265 HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG
SEQRES 6 A 265 GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER
SEQRES 7 A 265 VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY
SEQRES 8 A 265 LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP
SEQRES 9 A 265 ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS
SEQRES 10 A 265 VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY
SEQRES 11 A 265 VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU
SEQRES 12 A 265 ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU
SEQRES 13 A 265 LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR
SEQRES 14 A 265 TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS
SEQRES 15 A 265 ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN
SEQRES 16 A 265 GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS
SEQRES 17 A 265 PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL
SEQRES 18 A 265 SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN
SEQRES 19 A 265 ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS
SEQRES 20 A 265 PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR
SEQRES 21 A 265 THR ASP PHE LEU GLN
HET ZYC A 245 16
HET NA A 246 1
HET NA A 247 1
HET NA A 248 1
HET NA A 249 1
HET NA A 250 1
HET NA A 251 1
HET NA A 252 1
HET NA A 253 1
HET NA A 254 1
HET NA A 255 1
HET NA A 256 1
HET NA A 257 1
HET NA A 258 1
HET NA A 259 1
HET NA A 260 1
HET NA A 261 1
HET NA A 262 1
HET NA A 263 1
HET NA A 264 1
HET NA A 265 1
HET NA A 266 1
HET NA A 267 1
HET NA A 268 1
HET NA A 269 1
HET NA A 270 1
HET NA A 271 1
HET NA A 272 1
HET NA A 273 1
HET NA A 274 1
HET NA A 275 1
HET NA A 276 1
HET NA A 277 1
HET NA A 278 1
HET NA A 279 1
HET NA A 280 1
HET NA A 281 1
HET NA A 282 1
HET NA A 283 1
HET NA A 284 1
HET NA A 285 1
HET NA A 286 1
HET NA A 287 1
HET CL A 288 1
HET CL A 289 1
HET CL A 290 1
HET CL A 291 1
HET CL A 292 1
HET CL A 293 1
HET CL A 294 1
HET CL A 295 1
HET CL A 296 1
HET CL A 297 1
HET CL A 298 1
HET CL A 299 1
HET CL A 300 1
HET CL A 301 1
HET CL A 302 1
HET CL A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL A 306 1
HETNAM ZYC ETHYL (2E)-3-(4-HYDROXY-3-METHOXYPHENYL)PROP-2-ENOATE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETSYN ZYC ETHYL FERULATE
FORMUL 2 ZYC C12 H14 O4
FORMUL 3 NA 42(NA 1+)
FORMUL 45 CL 19(CL 1-)
FORMUL 64 HOH *173(H2 O)
HELIX 1 1 THR A 40 GLU A 53 1 14
HELIX 2 2 LYS A 71 MET A 75 5 5
HELIX 3 3 THR A 76 THR A 93 1 18
HELIX 4 4 ALA A 106 TYR A 119 1 14
HELIX 5 5 ALA A 133 GLY A 142 1 10
HELIX 6 6 GLY A 167 GLN A 175 1 9
HELIX 7 7 PRO A 177 ALA A 183 1 7
HELIX 8 8 PRO A 202 TYR A 212 1 11
HELIX 9 9 SER A 228 SER A 230 5 3
HELIX 10 10 TYR A 231 GLN A 244 1 14
SHEET 1 A 8 GLY A 0 ARG A 8 0
SHEET 2 A 8 LEU A 11 GLU A 19 -1 O GLU A 19 N GLY A 0
SHEET 3 A 8 ALA A 56 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 A 8 TYR A 25 PHE A 31 1 N ILE A 30 O VAL A 58
SHEET 5 A 8 VAL A 97 HIS A 105 1 O TYR A 101 N ILE A 29
SHEET 6 A 8 ILE A 123 LEU A 129 1 O LYS A 124 N ILE A 100
SHEET 7 A 8 VAL A 189 GLY A 194 1 O CYS A 190 N LEU A 128
SHEET 8 A 8 SER A 215 ILE A 220 1 O HIS A 218 N LEU A 191
SHEET 1 B 2 ASN A 143 THR A 144 0
SHEET 2 B 2 VAL A 147 THR A 148 -1 O VAL A 147 N THR A 144
SHEET 1 C 2 ARG A 157 PHE A 160 0
SHEET 2 C 2 LEU A 163 GLY A 166 -1 O LEU A 165 N LEU A 158
LINK NA NA A 282 O HOH A 479 1555 1555 2.39
LINK O ASP A 209 NA NA A 282 1555 1555 2.42
LINK O TYR A 212 NA NA A 282 1555 1555 2.46
LINK OG SER A 215 NA NA A 282 1555 1555 2.58
LINK NA NA A 272 O HOH A 477 1555 1555 2.64
LINK OD1 ASN A 63 NA NA A 276 1555 1555 2.67
LINK NA NA A 246 O HOH A 439 1555 1555 2.67
LINK NA NA A 263 O HOH A 388 1555 1555 2.71
LINK NA NA A 282 O HOH A 385 1555 1555 2.71
LINK NA NA A 275 O HOH A 413 1555 1555 2.72
LINK NA NA A 257 O HOH A 447 1555 1555 2.73
LINK NA NA A 275 O HOH A 388 1555 1555 2.73
LINK NA NA A 269 O HOH A 475 1555 1555 2.75
LINK NA NA A 250 O HOH A 423 1555 1555 2.76
LINK O ASP A 67 NA NA A 255 1555 1555 2.76
LINK NA NA A 267 O HOH A 348 1555 1555 2.77
LINK NA NA A 253 O HOH A 362 1555 1555 2.78
LINK NA NA A 263 O HOH A 353 1555 1555 2.80
LINK O GLN A 175 NA NA A 253 1555 1555 2.81
LINK O LYS A 71 NA NA A 276 1555 1555 2.82
LINK OD1 ASP A 69 NA NA A 255 1555 1555 2.84
LINK NA NA A 253 O HOH A 344 1555 1555 2.86
LINK O ARG A 157 NA NA A 258 1555 1555 2.87
LINK NA NA A 283 O HOH A 422 1555 1555 2.88
LINK NA NA A 258 O HOH A 441 1555 1555 2.88
LINK NA NA A 283 O HOH A 411 1555 1555 2.89
LINK NA NA A 283 O HOH A 352 1555 1555 2.92
LINK OD2AASP A 196 NA NA A 280 1555 1555 2.92
LINK NA NA A 277 O HOH A 355 1555 1555 2.96
LINK NA NA A 246 O HOH A 469 1555 1555 2.98
LINK NA NA A 267 O HOH A 467 1555 1555 3.00
LINK NA NA A 254 O HOH A 370 1555 1555 3.04
LINK O TYR A 149 NA NA A 271 1555 1555 3.06
LINK O GLN A -1 NA NA A 257 1555 1555 3.06
LINK O GLY A 142 NA NA A 271 1555 1555 3.07
LINK NA NA A 249 O HOH A 352 1555 1555 3.08
LINK OG1 THR A 198 NA NA A 284 1555 1555 3.10
LINK OE1 GLN A 12 NA NA A 255 1555 1555 3.10
LINK OE1 GLU A 180 NA NA A 264 1555 1555 3.10
LINK O PRO A 151 NA NA A 256 1555 1555 3.11
LINK OD2 ASP A 209 NA NA A 285 1555 1555 3.11
LINK O GLY A 222 NA NA A 280 1555 1555 3.11
LINK NA NA A 250 O HOH A 476 1555 1555 3.14
LINK OG1BTHR A 148 NA NA A 287 1555 1555 3.14
LINK NA NA A 285 O HOH A 426 1555 1555 3.14
LINK OE1 GLN A 210 NA NA A 259 1555 1555 3.18
LINK NA NA A 250 O HOH A 407 1555 1555 3.18
LINK NA NA A 282 O HOH A 438 1555 1555 3.20
SITE 1 AC1 12 GLY A 33 PHE A 34 ALA A 106 GLN A 107
SITE 2 AC1 12 LEU A 135 ASP A 138 THR A 144 GLN A 145
SITE 3 AC1 12 TYR A 169 HIS A 225 NA A 267 HOH A 338
SITE 1 AC2 6 LYS A 71 PHE A 72 GLU A 73 ASP A 162
SITE 2 AC2 6 HOH A 439 HOH A 469
SITE 1 AC3 1 GLU A 23
SITE 1 AC4 1 HOH A 352
SITE 1 AC5 2 GLN A 175 HOH A 423
SITE 1 AC6 1 LEU A 217
SITE 1 AC7 4 LEU A 219 ILE A 220 GLU A 221 CL A 288
SITE 1 AC8 3 GLN A 175 HOH A 344 HOH A 362
SITE 1 AC9 1 HOH A 370
SITE 1 BC1 3 GLN A 12 ASP A 67 ASP A 69
SITE 1 BC2 6 PRO A 151 ASP A 152 HIS A 153 ILE A 154
SITE 2 BC2 6 ARG A 171 HOH A 357
SITE 1 BC3 3 GLN A -1 PHE A -2 HOH A 447
SITE 1 BC4 3 ARG A 157 PRO A 159 HOH A 441
SITE 1 BC5 3 LYS A 206 ASP A 209 GLN A 210
SITE 1 BC6 2 GLU A 141 LYS A 233
SITE 1 BC7 2 MET A 1 ALA A 2
SITE 1 BC8 3 GLY A 137 HOH A 353 HOH A 388
SITE 1 BC9 5 LYS A 136 ILE A 178 TYR A 179 GLU A 180
SITE 2 BC9 5 CL A 303
SITE 1 CC1 1 GLY A 70
SITE 1 CC2 4 ALA A 36 ZYC A 245 HOH A 348 HOH A 467
SITE 1 CC3 1 CL A 302
SITE 1 CC4 2 CL A 305 HOH A 475
SITE 1 CC5 2 GLY A 66 CL A 301
SITE 1 CC6 5 GLU A 141 GLY A 142 THR A 148 TYR A 149
SITE 2 CC6 5 ASN A 237
SITE 1 CC7 4 SER A 228 ASP A 229 SER A 230 HOH A 477
SITE 1 CC8 1 ARG A 51
SITE 1 CC9 5 LYS A 136 CL A 300 CL A 303 HOH A 388
SITE 2 CC9 5 HOH A 413
SITE 1 DC1 4 ASN A 63 GLY A 70 LYS A 71 HOH A 346
SITE 1 DC2 4 CYS A 190 HIS A 218 PHE A 242 HOH A 355
SITE 1 DC3 2 GLY A 10 CL A 299
SITE 1 DC4 1 CL A 296
SITE 1 DC5 4 LYS A 124 ASP A 196 GLY A 222 TYR A 231
SITE 1 DC6 1 LEU A 217
SITE 1 DC7 5 ASP A 209 TYR A 212 SER A 215 HOH A 385
SITE 2 DC7 5 HOH A 479
SITE 1 DC8 3 HOH A 352 HOH A 411 HOH A 422
SITE 1 DC9 3 THR A 198 ASP A 224 HIS A 225
SITE 1 EC1 1 ASP A 209
SITE 1 EC2 1 CL A 298
SITE 1 EC3 2 GLY A 146 THR A 148
SITE 1 EC4 3 HIS A 153 NA A 252 HOH A 334
SITE 1 EC5 2 GLU A 180 CL A 294
SITE 1 EC6 3 SER A 41 ARG A 44 CL A 297
SITE 1 EC7 2 HOH A 377 HOH A 466
SITE 1 EC8 4 SER A 113 SER A 182 PHE A 185 TYR A 212
SITE 1 EC9 2 THR A 195 HOH A 459
SITE 1 FC1 1 CL A 289
SITE 1 FC2 3 ARG A 98 HOH A 435 HOH A 436
SITE 1 FC3 3 THR A 5 ASN A 214 NA A 279
SITE 1 FC4 2 ARG A 44 CL A 290
SITE 1 FC5 4 GLU A 45 GLN A 232 NA A 286 HOH A 378
SITE 1 FC6 1 NA A 278
SITE 1 FC7 4 TYR A 179 LYS A 207 NA A 275 HOH A 391
SITE 1 FC8 5 SER A 68 GLY A 70 NA A 270 HOH A 472
SITE 2 FC8 5 HOH A 473
SITE 1 FC9 1 NA A 268
SITE 1 GC1 3 LYS A 136 NA A 264 NA A 275
SITE 1 GC2 1 NA A 269
SITE 1 GC3 3 ASN A -5 LEU A -4 HIS A 96
CRYST1 71.872 85.396 81.142 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013914 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012324 0.00000
TER 1987 GLN A 244
MASTER 721 0 62 10 12 0 66 6 2201 1 88 21
END |